Tubulin gamma-1 chain (TUBG1)
The protein contains 451 amino acids for an estimated molecular weight of 51170 Da.
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| CDCBM4 | |
| CDCBM4 | |
| CDCBM4 | |
| dbSNP:rs13663 |
Biological Process
Cellular response to calcium ion
Ciliary basal body-plasma membrane docking
Cytoplasmic microtubule organization
G2/M transition of mitotic cell cycle
Meiotic spindle organization
Microtubule cytoskeleton organization
Microtubule nucleation
Microtubule-based process
Mitotic cell cycle
Mitotic sister chromatid segregation
Mitotic spindle organization
Organelle organization
Regulation of G2/M transition of mitotic cell cycle
Cellular Component
Apical part of cell
Cell leading edge
Centriole
Centrosome
Ciliary basal body
Condensed nuclear chromosome
Cytoplasm
Cytoplasmic microtubule
Cytosol
Gamma-tubulin complex
Microtubule
Mitotic spindle microtubule
Non-motile cilium
Nonmotile primary cilium
Nucleus
Pericentriolar material
Polar microtubule
Recycling endosome
Spindle
The reference OMIM entry for this protein is 191135
Tubulin, gamma-1; tubg1
Tubg
Tubulin-gamma complex-associated protein 1; tubgcp1
DESCRIPTION
The TUBG1 gene encodes gamma-tubulin, a structural component of the centrosome that associates with at least 6 other proteins to form the gamma-tubulin ring complex, which functions in microtubule nucleation (summary by Poirier et al., 2013).CLONING
Oakley and Oakley (1989) identified gamma-tubulin, which is essential for nuclear division and microtubule assembly in Aspergillus nidulans. By low stringency hybridizations, Zheng et al. (1991) cloned Drosophila and human cDNAs, the predicted products of which share more than 66% amino acid identity with A. nidulans gamma-tubulin. Gamma-tubulin-specific antibodies stained centrosomes of Drosophila, human, and mouse cell lines. Staining was most intense in prophase through metaphase when microtubule assembly from centrosomes was maximal. The findings suggested that gamma-tubulin is a universal component of microtubule organizing centers. Stearns et al. (1991) cloned and characterized gamma-tubulin genes from 5 other species, indicating further the ubiquitous and highly conserved nature of this protein. Gamma-tubulin is present at less than 1% the level of alpha- (see 602529) and beta-tubulins (see 602660) and is limited to the centrosome. In particular, it is associated with the pericentriolar material, the microtubule-nucleating material of the centrosome.MAPPING
Rommens et al. (1995) mapped the TUBG1 gene within a 700-kb region of a YAC of chromosome 17. By radiation hybrid analysis, Wise et al. (2000) mapped TUBG1 within 20 kb of TUBG2 (605785) at 17q21.GENE FUNCTION
Simerly et al. (1995) demonstrated by microscopy of inseminated human oocytes that the sperm introduces the centrosome. The centrosome then nucleates the new microtubule assembly to form the sperm aster, a step essential for successful fertilization. They showed further that oocytes from some infertile patients fail to complete fertilization because of defects in uniting the sperm and egg nuclei, indicating that failure to effect properly the cytoplasmic motions uniting the nuclei results in human infertility.BIOCHEMICAL FEATURES
- Crystal Structure Aldaz et al. (2005) reported the 2.7-angstrom crystal structure of human gamma-tubulin bound to GTP-gamma-S (a nonhydrolysable GTP analog). The authors observed a curved conformation for gamma-tubulin-GTP-gamma-S, similar to that seen for GDP-bound, unpolymerized alpha-beta-tubulin. Tubulins are thought to represent a distinct class of GTP-binding proteins, and conformational switching in gamma-tubulin might differ from the nucleotide-dependent switching of signaling GTPases. A crystal packing interaction replicates the lateral contacts between alpha- and beta-tubulins in the microtubule, and this association probably forms the basis for gamma-tubulin oligomerization within the gamma-tubulin ring complex. Laterally associated gamma-tubulins in the gamma-tubulin ring complex might promote microtubule nucleation by providing a template that enhances the intrinsically weak lateral interaction between alpha-beta-tubulin heterodimers. Because they are dimeric, alpha-beta-tubulins cannot form microtubule-like lateral associations in the curved conformation. The lateral array of gamma-tubulins they observed in the crystal revealed a unique functional property of a monomeric tubulin.MOLECULAR GENETICS
In 3 unrelated patients with complex cortical malformations-4 (CDCBM4; 615412), Poirier et al. (2013) ident ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for TUBG1
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 191135 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed